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O00418

- EF2K_HUMAN

UniProt

O00418 - EF2K_HUMAN

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Protein
Eukaryotic elongation factor 2 kinase
Gene
EEF2K
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Threonine kinase that regulates protein synthesis by controlling the rate of peptide chain elongation. Upon activation by a variety of upstream kinases including AMPK or TRPM7, phosphorylates the elongation factor EEF2 at a single site, renders it unable to bind ribosomes and thus inactive. In turn, the rate of protein synthesis is reduced.2 Publications

Catalytic activityi

ATP + [elongation factor 2] = ADP + [elongation factor 2] phosphate.1 Publication

Enzyme regulationi

Undergoes calcium/calmodulin-dependent intramolecular autophosphorylation, and this results in it becoming partially calcium/calmodulin-independent By similarity.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi296 – 3027ATP By similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. calcium ion binding Source: InterPro
  3. calmodulin binding Source: UniProtKB
  4. elongation factor-2 kinase activity Source: UniProtKB
  5. protein kinase activity Source: ProtInc
  6. translation factor activity, nucleic acid binding Source: ProtInc
Complete GO annotation...

GO - Biological processi

  1. insulin receptor signaling pathway Source: Reactome
  2. protein autophosphorylation Source: UniProtKB
  3. regulation of protein autophosphorylation Source: Ensembl
  4. translational elongation Source: ProtInc
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Ligandi

ATP-binding, Calcium, Calmodulin-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.11.20. 2681.
ReactomeiREACT_6772. S6K1 signalling.

Names & Taxonomyi

Protein namesi
Recommended name:
Eukaryotic elongation factor 2 kinase (EC:2.7.11.20)
Short name:
eEF-2 kinase
Short name:
eEF-2K
Alternative name(s):
Calcium/calmodulin-dependent eukaryotic elongation factor 2 kinase
Gene namesi
Name:EEF2K
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 16

Organism-specific databases

HGNCiHGNC:24615. EEF2K.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: ProtInc
  2. cytosol Source: Reactome
Complete GO annotation...

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi78 – 781S → A: Decreased kinase activity. 1 Publication
Mutagenesisi348 – 3481T → A: Decreased kinase activity. 1 Publication
Mutagenesisi366 – 3661S → A: Abrogates phosphorylation by RPS6KB1. 2 Publications
Mutagenesisi366 – 3661S → A: Decreased kinase activity. 2 Publications

Organism-specific databases

PharmGKBiPA134992891.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 725724Eukaryotic elongation factor 2 kinase
PRO_0000086936Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine1 Publication
Modified residuei18 – 181Phosphoserine6 Publications
Modified residuei61 – 611Phosphoserine; by autocatalysis1 Publication
Modified residuei66 – 661Phosphoserine; by autocatalysis1 Publication
Modified residuei71 – 711Phosphoserine By similarity
Modified residuei78 – 781Phosphoserine; by autocatalysis and TRPM72 Publications
Modified residuei348 – 3481Phosphothreonine; by autocatalysis3 Publications
Modified residuei353 – 3531Phosphothreonine; by autocatalysis1 Publication
Modified residuei359 – 3591Phosphoserine; by MAPK13 and CDK12 Publications
Modified residuei366 – 3661Phosphoserine; by autocatalysis, RPS6KA1 and RPS6KB12 Publications
Modified residuei398 – 3981Phosphoserine; by AMPK1 Publication
Modified residuei445 – 4451Phosphoserine; by autocatalysis3 Publications
Modified residuei470 – 4701Phosphoserine3 Publications
Modified residuei474 – 4741Phosphoserine; by autocatalysis4 Publications
Modified residuei477 – 4771Phosphoserine1 Publication
Modified residuei491 – 4911Phosphoserine; by autocatalysis1 Publication
Modified residuei500 – 5001Phosphoserine; by PKA By similarity

Post-translational modificationi

Autophosphorylated at multiple residues, Thr-348 being the major site. Phosphorylated by AMP-activated protein kinase AMPK at Ser-398 leading to EEF2K activation and protein synthesis inhibition. Phosphorylated by TRPM7 at Ser-78 resulting in improved protein stability, higher EE2F phosphorylated and subsequently reduced rate of protein synthesis. Phosphorylation by other kinases such as CDK1 and MAPK13 at Ser-359 or RPS6KA1 and RPS6KB1 at Ser-366 instead decrease EEF2K activity and promote protein synthesis.7 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiO00418.
PaxDbiO00418.
PRIDEiO00418.

PTM databases

PhosphoSiteiO00418.

Expressioni

Gene expression databases

ArrayExpressiO00418.
BgeeiO00418.
CleanExiHS_EEF2K.
GenevestigatoriO00418.

Organism-specific databases

HPAiCAB007818.

Interactioni

Subunit structurei

Monomer or homodimer Reviewed prediction.

Protein-protein interaction databases

BioGridi118953. 33 interactions.
IntActiO00418. 10 interactions.
MINTiMINT-207181.
STRINGi9606.ENSP00000263026.

Structurei

3D structure databases

ProteinModelPortaliO00418.
SMRiO00418. Positions 117-323, 527-645.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini116 – 326211Alpha-type protein kinase
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni594 – 61017Calmodulin-binding Reviewed prediction
Add
BLAST
Regioni610 – 62718Pseudosubstrate/autoinhibitory domain Reviewed prediction
Add
BLAST

Domaini

The catalytic domain is located to N-terminal region. The neighbor region contains the calmodulin-binding domain.1 Publication

Sequence similaritiesi

Phylogenomic databases

eggNOGiNOG145133.
HOGENOMiHOG000022023.
HOVERGENiHBG002318.
InParanoidiO00418.
KOiK08292.
OMAiQIHTETG.
OrthoDBiEOG7673B0.
PhylomeDBiO00418.
TreeFamiTF316085.

Family and domain databases

Gene3Di1.25.40.10. 1 hit.
InterProiIPR017400. Elongation_factor_2_kinase.
IPR011009. Kinase-like_dom.
IPR004166. MHCK_EF2_kinase.
IPR006597. Sel1-like.
IPR011990. TPR-like_helical.
[Graphical view]
PfamiPF02816. Alpha_kinase. 1 hit.
PF08238. Sel1. 4 hits.
[Graphical view]
PIRSFiPIRSF038139. Elongation_factor_2_kinase. 1 hit.
SMARTiSM00811. Alpha_kinase. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS51158. ALPHA_KINASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

O00418-1 [UniParc]FASTAAdd to Basket

« Hide

MADEDLIFRL EGVDGGQSPR AGHDGDSDGD SDDEEGYFIC PITDDPSSNQ    50
NVNSKVNKYY SNLTKSERYS SSGSPANSFH FKEAWKHAIQ KAKHMPDPWA 100
EFHLEDIATE RATRHRYNAV TGEWLDDEVL IKMASQPFGR GAMRECFRTK 150
KLSNFLHAQQ WKGASNYVAK RYIEPVDRDV YFEDVRLQME AKLWGEEYNR 200
HKPPKQVDIM QMCIIELKDR PGKPLFHLEH YIEGKYIKYN SNSGFVRDDN 250
IRLTPQAFSH FTFERSGHQL IVVDIQGVGD LYTDPQIHTE TGTDFGDGNL 300
GVRGMALFFY SHACNRICES MGLAPFDLSP RERDAVNQNT KLLQSAKTIL 350
RGTEEKCGSP QVRTLSGSRP PLLRPLSENS GDENMSDVTF DSLPSSPSSA 400
TPHSQKLDHL HWPVFSDLDN MASRDHDHLD NHRESENSGD SGYPSEKRGE 450
LDDPEPREHG HSYSNRKYES DEDSLGSSGR VCVEKWNLLN SSRLHLPRAS 500
AVALEVQRLN ALDLEKKIGK SILGKVHLAM VRYHEGGRFC EKGEEWDQES 550
AVFHLEHAAN LGELEAIVGL GLMYSQLPHH ILADVSLKET EENKTKGFDY 600
LLKAAEAGDR QSMILVARAF DSGQNLSPDR CQDWLEALHW YNTALEMTDC 650
DEGGEYDGMQ DEPRYMMLAR EAEMLFTGGY GLEKDPQRSG DLYTQAAEAA 700
MEAMKGRLAN QYYQKAEEAW AQMEE 725
Length:725
Mass (Da):82,144
Last modified:July 28, 2009 - v2
Checksum:i9D2900E50EFF12DA
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti23 – 231H → R.2 Publications
Corresponds to variant rs9935059 [ dbSNP | Ensembl ].
VAR_033915
Natural varianti75 – 751P → A.1 Publication
Corresponds to variant rs17841292 [ dbSNP | Ensembl ].
VAR_033916
Natural varianti291 – 2911T → M in a colorectal adenocarcinoma sample; somatic mutation. 1 Publication
VAR_041534
Natural varianti361 – 3611Q → R.2 Publications
Corresponds to variant rs4783453 [ dbSNP | Ensembl ].
VAR_058405
Natural varianti433 – 4331R → W.1 Publication
Corresponds to variant rs56137739 [ dbSNP | Ensembl ].
VAR_041535
Natural varianti609 – 6091D → H.1 Publication
VAR_041536

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U93850 mRNA. Translation: AAB58270.1.
AC009034 Genomic DNA. No translation available.
BC032665 mRNA. Translation: AAH32665.1.
CCDSiCCDS10604.1.
RefSeqiNP_037434.1. NM_013302.3.
XP_005276554.1. XM_005276497.1.
UniGeneiHs.498892.

Genome annotation databases

EnsembliENST00000263026; ENSP00000263026; ENSG00000103319.
GeneIDi101930123.
29904.
KEGGihsa:101930123.
hsa:29904.
UCSCiuc002dki.3. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U93850 mRNA. Translation: AAB58270.1 .
AC009034 Genomic DNA. No translation available.
BC032665 mRNA. Translation: AAH32665.1 .
CCDSi CCDS10604.1.
RefSeqi NP_037434.1. NM_013302.3.
XP_005276554.1. XM_005276497.1.
UniGenei Hs.498892.

3D structure databases

ProteinModelPortali O00418.
SMRi O00418. Positions 117-323, 527-645.
ModBasei Search...

Protein-protein interaction databases

BioGridi 118953. 33 interactions.
IntActi O00418. 10 interactions.
MINTi MINT-207181.
STRINGi 9606.ENSP00000263026.

Chemistry

BindingDBi O00418.
ChEMBLi CHEMBL5026.
GuidetoPHARMACOLOGYi 2014.

PTM databases

PhosphoSitei O00418.

Proteomic databases

MaxQBi O00418.
PaxDbi O00418.
PRIDEi O00418.

Protocols and materials databases

DNASUi 29904.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000263026 ; ENSP00000263026 ; ENSG00000103319 .
GeneIDi 101930123.
29904.
KEGGi hsa:101930123.
hsa:29904.
UCSCi uc002dki.3. human.

Organism-specific databases

CTDi 29904.
GeneCardsi GC16P022217.
HGNCi HGNC:24615. EEF2K.
HPAi CAB007818.
MIMi 606968. gene.
neXtProti NX_O00418.
PharmGKBi PA134992891.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG145133.
HOGENOMi HOG000022023.
HOVERGENi HBG002318.
InParanoidi O00418.
KOi K08292.
OMAi QIHTETG.
OrthoDBi EOG7673B0.
PhylomeDBi O00418.
TreeFami TF316085.

Enzyme and pathway databases

BRENDAi 2.7.11.20. 2681.
Reactomei REACT_6772. S6K1 signalling.

Miscellaneous databases

GeneWikii EEF2K.
NextBioi 52478.
PROi O00418.
SOURCEi Search...

Gene expression databases

ArrayExpressi O00418.
Bgeei O00418.
CleanExi HS_EEF2K.
Genevestigatori O00418.

Family and domain databases

Gene3Di 1.25.40.10. 1 hit.
InterProi IPR017400. Elongation_factor_2_kinase.
IPR011009. Kinase-like_dom.
IPR004166. MHCK_EF2_kinase.
IPR006597. Sel1-like.
IPR011990. TPR-like_helical.
[Graphical view ]
Pfami PF02816. Alpha_kinase. 1 hit.
PF08238. Sel1. 4 hits.
[Graphical view ]
PIRSFi PIRSF038139. Elongation_factor_2_kinase. 1 hit.
SMARTi SM00811. Alpha_kinase. 1 hit.
[Graphical view ]
SUPFAMi SSF56112. SSF56112. 1 hit.
PROSITEi PS51158. ALPHA_KINASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, VARIANT ARG-361.
    Tissue: Glial tumor.
  2. "The sequence and analysis of duplication-rich human chromosome 16."
    Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J.
    , Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M., Rubin E.M., Pennacchio L.A.
    Nature 432:988-994(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANTS ARG-23 AND ARG-361.
    Tissue: Lymph.
  4. "Mapping the functional domains of elongation factor-2 kinase."
    Pavur K.S., Petrov A.N., Ryazanov A.G.
    Biochemistry 39:12216-12224(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: AUTOPHOSPHORYLATION, DOMAIN.
  5. "A novel method to identify protein kinase substrates: eEF2 kinase is phosphorylated and inhibited by SAPK4/p38delta."
    Knebel A., Morrice N., Cohen P.
    EMBO J. 20:4360-4369(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-359.
  6. "Regulation of elongation factor 2 kinase by p90(RSK1) and p70 S6 kinase."
    Wang X., Li W., Williams M., Terada N., Alessi D.R., Proud C.G.
    EMBO J. 20:4370-4379(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-366 BY RPS6KA1 AND RPS6KB1, MUTAGENESIS OF SER-366.
  7. "Robust phosphoproteomic profiling of tyrosine phosphorylation sites from human T cells using immobilized metal affinity chromatography and tandem mass spectrometry."
    Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M., Peters E.C.
    Anal. Chem. 76:2763-2772(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  8. "Stimulation of the AMP-activated protein kinase leads to activation of eukaryotic elongation factor 2 kinase and to its phosphorylation at a novel site, serine 398."
    Browne G.J., Finn S.G., Proud C.G.
    J. Biol. Chem. 279:12220-12231(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, PHOSPHORYLATION AT SER-398.
  9. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
    Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
    Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18 AND SER-474, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
    Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
    Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18 AND SER-445, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. "cdc2-cyclin B regulates eEF2 kinase activity in a cell cycle- and amino acid-dependent manner."
    Smith E.M., Proud C.G.
    EMBO J. 27:1005-1016(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-359.
  12. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-348; SER-470; SER-474 AND SER-477, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  13. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  15. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18; THR-348; SER-445; SER-470 AND SER-474, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  16. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  17. "The channel-kinase TRPM7 regulates phosphorylation of the translational factor eEF2 via eEF2-k."
    Perraud A.L., Zhao X., Ryazanov A.G., Schmitz C.
    Cell. Signal. 23:586-593(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-78.
  18. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18 AND SER-470, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  19. "Identification of autophosphorylation sites in eukaryotic elongation factor-2 kinase."
    Pyr Dit Ruys S., Wang X., Smith E.M., Herinckx G., Hussain N., Rider M.H., Vertommen D., Proud C.G.
    Biochem. J. 442:681-692(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-61; SER-66; SER-78; THR-348; THR-353; SER-366; SER-445; SER-474 AND SER-491, MUTAGENESIS OF SER-78; THR-348 AND SER-366.
  20. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
    Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
    Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  21. "Patterns of somatic mutation in human cancer genomes."
    Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G.
    , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.
    Nature 446:153-158(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS [LARGE SCALE ANALYSIS] ARG-23; ALA-75; MET-291; TRP-433 AND HIS-609.

Entry informationi

Entry nameiEF2K_HUMAN
AccessioniPrimary (citable) accession number: O00418
Secondary accession number(s): Q8N588
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: July 28, 2009
Last modified: September 3, 2014
This is version 138 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 16
    Human chromosome 16: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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